Article abstract


Nature Structural & Molecular Biology 14, 60 - 67 (2007)
Published online: 31 December 2006 | Corrected online: 19 January 2007 | doi:10.1038/nsmb1188



There is a Corrigendum (February 2007) associated with this Article.

Nucleotide recognition by the cytoplasmic domain of the human chloride transporter ClC-5

Sebastian Meyer1, Sara Savaresi1, Ian C Forster2 & Raimund Dutzler1


The ubiquitous CBS domains, which are found as part of cytoplasmic domains in the ClC family of chloride channels and transporters, have previously been identified as building blocks for regulatory nucleotide-binding sites. Here we report the structures of the cytoplasmic domain of the human transporter ClC-5 in complex with ATP and ADP. The nucleotides bind to a specific site in the protein. As determined by equilibrium dialysis, the affinities for ATP, ADP and AMP are in the high micromolar range. Point mutations that interfere with nucleotide binding change the transport behavior of a ClC-5 mutant expressed in Xenopus laevis oocytes. Our results establish the structural and energetic basis for the interaction of ClC-5 with nucleotides and provide a framework for future investigations.

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  1. Department of Biochemistry, University of Zurich, Winterthurer Strasse 190, CH-8057 Zurich, Switzerland.
  2. Institute of Physiology, University of Zurich, Winterthurer Strasse 190, CH-8057 Zurich, Switzerland.

Correspondence to: Raimund Dutzler1 e-mail: dutzler@bioc.unizh.ch.

* In the version of this article initially published, Figure 4 contained an error. The legend labels placed within Figure 4d were exchanged. The error has been corrected in the HTML and PDF versions of this article.

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